MG1655
W3110
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Gene Report : dnaJ
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)
Acta Microbiol Pol. 1997;46(1):7-17.
Escherichia coli defects caused by null mutations in dnaK and dnaJ genes.
Paciorek J, Kardys K, Lobacz B, Wolska KI. ( 9271843 )
     Deletion OCR27 (D)  ,  OCR27-6 (D)  ,  OCR27-7 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  dnaJ
Related strains
     Strains Search Search strains by gene name:  dnaJ   Search strains by all related name:  dnaJ b0015 ECK0015 faa groA groB groC groP grpC JW0014

General information  (Go to Linear View:)
 Gene Name dnaJ  
 Alternative name b0015,ECK0015,faa,groA,groB,groC,groP,grpC,JW0014  
 Location, Length 14,168 - 15,298 (  +  ) ;   0.31 min ; 1131 (bp) ,   376 (aa) Go to Linear View
 Product chaperone Hsp40, co-chaperone with DnaK  
 Operon Name dnaK-tpke11-dnaJ  
 Note chaperone with DnaK; heat shock protein; GO_component: GO:0005737 - cytoplasm; GO_process: GO:0006457 - protein folding  
 Function factor; Chaperones  
 Gene Ontology GO:0005524 ; ATP binding ( dnaJ )
GO:0005737 ; cytoplasm ( dnaJ )
GO:0006260 ; DNA replication ( dnaJ )
GO:0006457 ; protein folding ( dnaJ )
GO:0006950 ; response to stress ( dnaJ )
GO:0008270 ; zinc ion binding ( dnaJ )
GO:0009408 ; response to heat ( dnaJ )
GO:0031072 ; heat shock protein binding ( dnaJ )
GO:0046872 ; metal ion binding ( dnaJ )
GO:0051082 ; unfolded protein binding ( dnaJ )
 PID 1786197  
 EC number
  (KEGG Pathway)
 
 
Verified Protein Starts (data compiled from literature and appropriate citations are available from EcoGene)
     EcoGene dnaJ ( EG10240 )  
    Number of removed 1 aa cleaved  
SWISS-PROT  ( Show simple )
  botton Entry name(Acc.no) DNAB_ECOLI ( P03005 )
    -  Protein name Replicative DNA helicase  
    -  Synonyms EC 3.6.1.-  
    -  Gene name OrderedLocusNames=b4052, SF4154, S3577;  
    -  Comments
  • FUNCTION:Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with dnaC protein, primase, and other prepriming proteins.
  • SUBUNIT:Homohexamer.
  • SIMILARITY:Belongs to the helicase family. DnaB subfamily.  
  •   botton Entry name(Acc.no) DNAK_ECOLI ( P04475 )
        -  Protein name Chaperone protein dnaK  
        -  Synonyms Heat shock protein 70, Heat shock 70 kDa protein, HSP70  
        -  Gene name OrderedLocusNames=b0014, c0019, z0014, ECs0014;  
        -  Comments
  • FUNCTION:Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the dnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the dnaA protein. Also participates actively in the response to hyperosmotic shock.
  • PTM:Autophosphorylated; grpE inhibits the autophosphorylation.
  • MISCELLANEOUS:The mutants dnaK756(Ts), seg-1 and seg-2 confer temperature sensitivity.
  • SIMILARITY:Belongs to the heat shock protein 70 family.  
  •   botton Entry name(Acc.no) DNAJ_ECOLI ( P08622 )
        -  Protein name Chaperone protein dnaJ  
        -  Synonyms Heat shock protein J, HSP40  
        -  Gene name Name=dnaJ; Synonyms=groP; OrderedLocusNames=b0015;  
        -  Comments
  • FUNCTION:Interacts with dnaK to disassemble a protein complex at the phage lambda origin of replication. Stimulates, jointly with grpE, the ATPase activity of dnaK.
  • COFACTOR:Binds 2 zinc ions per monomer.
  • SUBUNIT:Homodimer.
  • SUBCELLULAR LOCATION:Cytoplasmic.
  • INDUCTION:By heat shock under the control of the htpR regulatory protein.
  • SIMILARITY:Belongs to the dnaJ family.
  • SIMILARITY:Contains 1 CR domain.
  • SIMILARITY:Contains 1 J domain.  
  •   botton Entry name(Acc.no) Q8FLC5 ( Q8FLC5 )
        -  Protein name Chaperone protein dnaJ.  
        -  Synonyms  
        -  Gene name Name=dnaJ; OrderedLocusNames=c0020;  
        -  Comments
  • FUNCTION:Acts as a co-chaperone. Stimulates, jointly with grpE, the ATPase activity of dnaK (By similarity).
  • COFACTOR:Binds 2 zinc ions per monomer (By similarity).
  • SUBCELLULAR LOCATION:Cytoplasmic (By similarity).
  • SIMILARITY:Belongs to the dnaJ family.  
  •   botton Entry name(Acc.no) Q8XA65 ( Q8XA65 )
        -  Protein name Chaperone with DnaK; heat shock protein.  
        -  Synonyms  
        -  Gene name Name=dnaJ; OrderedLocusNames=z0015;  
        -  Comments
  • FUNCTION:Acts as a co-chaperone. Stimulates, jointly with grpE, the ATPase activity of dnaK (By similarity).
  • COFACTOR:Binds 2 zinc ions per monomer (By similarity).
  • SUBCELLULAR LOCATION:Cytoplasmic (By similarity).
  • SIMILARITY:Belongs to the dnaJ family.  

  •  Linear View (Whole Mode)
    View Location
       5.0  –  30.0 (KBP)

    Homology Analysis
    BLAST
        Bacteria
             GTOP dnaJ (  homologous genes of other bacterias  )  
        PDB     (database updated : 2007.02.20 )
             PSI-BLAST Chain A, The Crystal Structure Of Hsp40 Ydj1  
        SWISS-PROT     (database updated : 2007.02.20 )
             BLAST Chaperone protein dnaJ  
             PSI-BLAST Chaperone protein dnaJ
        nr     (database updated : 2007.02.20 )
             BLAST chaperone with DnaK; heat shock protein [Shigella flexneri 2a str. 2457T]  
    Pfam 28.0   (database updated : 2015-05 )
        Pfam
    PROSITE
        PROSITE PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    TYR_PHOSPHO_SITE    MYRISTYL    CYTOCHROME_C    DNAJ_1    DNAJ_CXXCXGXG     

    Other Cross-Reference
        COG COG0484O 
        EcoCyc dnaJ 

    MMBR References
    Proc Natl Acad Sci U S A. 1971;68:2977-2981
    Bacterial mutants in which the gene N function of bacteriophage lambda is blocked have an altered RNA polymerase.
    Georgopoulos, C.
    J Biol Chem. 1996;271:30798-30803
    Role of the heat shock protein DnaJ in the lon-dependent degradation of naturally unstable proteins.
    Jubete, Y., M. R. Maurizi, and S. Gottesman.
    J Biol Chem. 1986;261:1782-1785
    The nucleotide sequence of the Escherichia coli K12 and dnaJ+ gene: a gene that encodes a heat shock protein.
    Bardwell, J. C., K. Tilly, E. A. Craig, J. King, M. Zylicz, and C. Georgopoulos.
    J Biol Chem. 1986;261:1778-1781
    Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product.
    Ohki, M., F. Tamura, S. Nishimura, and H. Uchida.
    Biochim Biophys Acta. 1989;1009(1):94-8.
    A complete deletion mutant of the Escherichia coli dnaKdnaJ operon.
    Ohki R, Morita R, Kawamata T, Uchida H, Ohki M. ( 2675977 )
    J Biol Chem. 1992;267:13180-13184
    Escherichia coli dnaJ deletion mutation results in loss of stability of a positive regulator, CRP.
    Ohki, R., T. Kawamata, Y. Katoh, F. Hosoda, and M. Ohki.
    Eur J Biochem. 1973;35(2):331-7.
    Biochemical and immunological characterization of threonyl-tRNA synthetase of two borrelidin-resistant mutants of Escherichia coli K12.
    Paetz W, Nass G. ( 4577856 )
    J Mol Biol. 1977;113(1):1-25.
    Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12.
    Saito H, Uchida H. ( 328896 )
    Genes Dev. 1990;4:2202-2209
    DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32.
    Straus, D., W. Walter, and C. A. Gross.
    Mol Gen Genet. 1977;151(1):27-34.
    A new host gene (groPC) necessary for lambda DNA replication.
    Sunshine M, Feiss M, Stuart J, Yochem J. ( 325364 )
    Mol Gen Genet. 1983;192(1-2):10-4.
    Genetic characterization of a gene for prolipoprotein signal peptidase in Escherichia coli.
    Yamagata H, Taguchi N, Daishima K, Mizushima S. ( 6227793 )
    J Biol Chem. 1995;270:22669-22672
    A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase.
    de Crouy-Chanel, A., M. Kohiyama, and G. Richarme.

    Sequences
    Amino acid
    FASTA format
    0001 MAKQDYYEIL GVSKTAEERE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDS QKRAAYDQYG 
    0071 HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYN MELTLEEAVR GVTKEIRIPT 
    0141 LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ QTCPHCQGRG TLIKDPCNKC HGHGRVERSK 
    0211 TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP AGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI 
    0281 EVPTLDGRVK LKVPGETQTG KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG 
    0351 PTGEHNSPRS KSFFDGVKKF FDDLTR
    
    
    Nucleotide
    FASTA format

    View sequence out neighbor 100bp
    -100                                             GACAAAAAAT AATCGCCCTA TAAACGGGTA 
    -070 ATTATACTGA CACGGGCGAA GGGGAATTTC CTCTCCGCCC GTGCATTCAT CTAGGGGCAA TTTAAAAAAG 
    0001 atggctaagc aagattatta cgagatttta ggcgtttcca aaacagcgga agagcgtgaa atcagaaagg 
    0071 cctacaaacg cctggccatg aaataccacc cggaccgtaa ccagggtgac aaagaggccg aggcgaaatt 
    0141 taaagagatc aaggaagctt atgaagttct gaccgactcg caaaaacgtg cggcatacga tcagtatggt 
    0211 catgctgcgt ttgagcaagg tggcatgggc ggcggcggtt ttggcggcgg cgcagacttc agcgatattt 
    0281 ttggtgacgt tttcggcgat atttttggcg gcggacgtgg tcgtcaacgt gcggcgcgcg gtgctgattt 
    0351 acgctataac atggagctca ccctcgaaga agctgtacgt ggcgtgacca aagagatccg cattccgact 
    0421 ctggaagagt gtgacgtttg ccacggtagc ggtgcaaaac caggtacaca gccgcagact tgtccgacct 
    0491 gtcatggttc tggtcaggtg cagatgcgcc agggattctt cgctgtacag cagacctgtc cacactgtca 
    0561 gggccgcggt acgctgatca aagatccgtg caacaaatgt catggtcatg gtcgtgttga gcgcagcaaa 
    0631 acgctgtccg ttaaaatccc ggcaggggtg gacactggag accgcatccg tcttgcgggc gaaggtgaag 
    0701 cgggcgagca tggcgcaccg gcaggcgatc tgtacgttca ggttcaggtt aaacagcacc cgattttcga 
    0771 gcgtgaaggc aacaacctgt attgcgaagt cccgatcaac ttcgctatgg cggcgctggg tggcgaaatc 
    0841 gaagtaccga cccttgatgg tcgcgtcaaa ctgaaagtgc ctggcgaaac ccagaccggt aagctattcc 
    0911 gtatgcgcgg taaaggcgtc aagtctgtcc gcggtggcgc acagggtgat ttgctgtgcc gcgttgtcgt 
    0981 cgaaacaccg gtaggcctga acgaaaggca gaaacagctg ctgcaagagc tgcaagaaag cttcggtggc 
    1051 ccaaccggcg agcacaacag cccgcgctca aagagcttct ttgatggtgt gaagaagttt tttgacgacc 
    1121 tgacccgcta aCCTCCCCAA AAGCCTGCCC GTGGGCAGGC CTGGGTAAAA ATAGGGTGCG TTGAAGATAT 
    1191 GCGAGCACCT GTAAAGTGGC GGGGATCACT CCCATAAGCG C